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Protein

DNA topoisomerase 2

Gene

TOP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes.2 Publications

Miscellaneous

In yeast topoisomerase II can substitute topoisomerase I for the relaxing activity.
Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.
Present with 5730 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.PROSITE-ProRule annotation3 Publications

Cofactori

Mg2+PROSITE-ProRule annotation2 Publications, Mn2+PROSITE-ProRule annotation2 Publications, Ca2+PROSITE-ProRule annotation2 PublicationsNote: Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ or Ca2+.PROSITE-ProRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei70ATP1 Publication1
Binding sitei99ATP1 Publication1
Metal bindingi449Magnesium 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi526Magnesium 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi526Magnesium 2PROSITE-ProRule annotation1 Publication1
Metal bindingi528Magnesium 2PROSITE-ProRule annotation1 Publication1
Sitei781Transition state stabilizer1
Active sitei782O-(5'-phospho-DNA)-tyrosine intermediate2 Publications1
Sitei833Important for DNA bending; intercalates between base pairs of target DNA1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi127 – 129ATP1 Publication3
Nucleotide bindingi140 – 147ATP1 Publication8
Nucleotide bindingi365 – 367ATP1 Publication3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • DNA topoisomerase type II (ATP-hydrolyzing) activity Source: SGD
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Isomerase, Topoisomerase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33117-MONOMER
BRENDAi5.99.1.3 984
ReactomeiR-SCE-4615885 SUMOylation of DNA replication proteins

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 2 (EC:5.99.1.3)
Alternative name(s):
DNA topoisomerase II
Gene namesi
Name:TOP2
Synonyms:TOR3
Ordered Locus Names:YNL088W
ORF Names:N2244
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL088W
SGDiS000005032 TOP2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi333 – 336KKKK → AAAA: Reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. 4
Mutagenesisi333 – 336KKKK → AEEA: Strongly reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. 4
Mutagenesisi690R → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi697D → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi700K → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi704R → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi736H → A: No effect. 1 Publication1
Mutagenesisi781R → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi782Y → F: Loss of enzyme activity. 1 Publication1
Mutagenesisi828N → A: Strongly reduced enzyme activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5290

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001453871 – 1428DNA topoisomerase 2Add BLAST1428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1086Phosphothreonine; by CK21 Publication1
Modified residuei1087Phosphoserine; by CK21 Publication1
Modified residuei1252PhosphoserineCombined sources1
Modified residuei1258Phosphothreonine; by CK21 Publication1
Modified residuei1266Phosphoserine; by CK21 Publication1
Modified residuei1269Phosphoserine; by CK21 Publication1
Modified residuei1272Phosphoserine; by CK21 Publication1
Modified residuei1353Phosphoserine; by CK21 Publication1
Modified residuei1356Phosphoserine; by CK21 Publication1
Modified residuei1408Phosphoserine; by CK21 Publication1
Modified residuei1423Phosphoserine; by CK21 Publication1

Post-translational modificationi

Phosphorylation enhances the activity. Stimulates decatenation activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP06786
PaxDbiP06786
PRIDEiP06786

PTM databases

iPTMnetiP06786

Interactioni

Subunit structurei

Homodimer.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei477Interaction with DNAPROSITE-ProRule annotation1
Sitei480Interaction with DNA1 Publication1
Sitei650Interaction with DNA1 Publication1
Sitei651Interaction with DNA1 Publication1
Sitei700Interaction with DNA1 Publication1
Sitei734Interaction with DNAPROSITE-ProRule annotation1
Sitei740Interaction with DNAPROSITE-ProRule annotation1
Sitei908Interaction with DNAPROSITE-ProRule annotation1

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi35735, 222 interactors
DIPiDIP-2300N
IntActiP06786, 34 interactors
MINTiP06786
STRINGi4932.YNL088W

Structurei

Secondary structure

11428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00076
ProteinModelPortaliP06786
SMRiP06786
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06786

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini443 – 557ToprimPROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni333 – 336Interaction with DNA1 Publication4
Regioni965 – 974Interaction with DNA1 Publication10

Sequence similaritiesi

Belongs to the type II topoisomerase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000016222
HOGENOMiHOG000216693
InParanoidiP06786
KOiK03164
OMAiACKLPNY
OrthoDBiEOG092C08KH

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
cd00187 TOP4c, 1 hit
cd03365 TOPRIM_TopoIIA, 1 hit
Gene3Di3.30.230.10, 1 hit
3.30.565.10, 1 hit
3.40.50.670, 2 hits
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR001241 Topo_IIA
IPR013760 Topo_IIA-like_dom_sf
IPR002205 Topo_IIA_A/C
IPR013759 Topo_IIA_B_C
IPR013506 Topo_IIA_bsu_dom2
IPR018522 TopoIIA_CS
IPR031660 TOPRIM_C
IPR006171 TOPRIM_domain
IPR034157 TOPRIM_TopoII
PANTHERiPTHR10169 PTHR10169, 1 hit
PfamiView protein in Pfam
PF00204 DNA_gyraseB, 1 hit
PF00521 DNA_topoisoIV, 1 hit
PF02518 HATPase_c, 1 hit
PF01751 Toprim, 1 hit
PF16898 TOPRIM_C, 1 hit
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SM00433 TOP2c, 1 hit
SM00434 TOP4c, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
SSF56719 SSF56719, 1 hit
PROSITEiView protein in PROSITE
PS00177 TOPOISOMERASE_II, 1 hit
PS50880 TOPRIM, 1 hit

Sequencei

Sequence statusi: Complete.

P06786-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTEPVSASD KYQKISQLEH ILKRPDTYIG SVETQEQLQW IYDEETDCMI
60 70 80 90 100
EKNVTIVPGL FKIFDEILVN AADNKVRDPS MKRIDVNIHA EEHTIEVKND
110 120 130 140 150
GKGIPIEIHN KENIYIPEMI FGHLLTSSNY DDDEKKVTGG RNGYGAKLCN
160 170 180 190 200
IFSTEFILET ADLNVGQKYV QKWENNMSIC HPPKITSYKK GPSYTKVTFK
210 220 230 240 250
PDLTRFGMKE LDNDILGVMR RRVYDINGSV RDINVYLNGK SLKIRNFKNY
260 270 280 290 300
VELYLKSLEK KRQLDNGEDG AAKSDIPTIL YERINNRWEV AFAVSDISFQ
310 320 330 340 350
QISFVNSIAT TMGGTHVNYI TDQIVKKISE ILKKKKKKSV KSFQIKNNMF
360 370 380 390 400
IFINCLIENP AFTSQTKEQL TTRVKDFGSR CEIPLEYINK IMKTDLATRM
410 420 430 440 450
FEIADANEEN ALKKSDGTRK SRITNYPKLE DANKAGTKEG YKCTLVLTEG
460 470 480 490 500
DSALSLAVAG LAVVGRDYYG CYPLRGKMLN VREASADQIL KNAEIQAIKK
510 520 530 540 550
IMGLQHRKKY EDTKSLRYGH LMIMTDQDHD GSHIKGLIIN FLESSFPGLL
560 570 580 590 600
DIQGFLLEFI TPIIKVSITK PTKNTIAFYN MPDYEKWREE ESHKFTWKQK
610 620 630 640 650
YYKGLGTSLA QEVREYFSNL DRHLKIFHSL QGNDKDYIDL AFSKKKADDR
660 670 680 690 700
KEWLRQYEPG TVLDPTLKEI PISDFINKEL ILFSLADNIR SIPNVLDGFK
710 720 730 740 750
PGQRKVLYGC FKKNLKSELK VAQLAPYVSE CTAYHHGEQS LAQTIIGLAQ
760 770 780 790 800
NFVGSNNIYL LLPNGAFGTR ATGGKDAAAA RYIYTELNKL TRKIFHPADD
810 820 830 840 850
PLYKYIQEDE KTVEPEWYLP ILPMILVNGA EGIGTGWSTY IPPFNPLEII
860 870 880 890 900
KNIRHLMNDE ELEQMHPWFR GWTGTIEEIE PLRYRMYGRI EQIGDNVLEI
910 920 930 940 950
TELPARTWTS TIKEYLLLGL SGNDKIKPWI KDMEEQHDDN IKFIITLSPE
960 970 980 990 1000
EMAKTRKIGF YERFKLISPI SLMNMVAFDP HGKIKKYNSV NEILSEFYYV
1010 1020 1030 1040 1050
RLEYYQKRKD HMSERLQWEV EKYSFQVKFI KMIIEKELTV TNKPRNAIIQ
1060 1070 1080 1090 1100
ELENLGFPRF NKEGKPYYGS PNDEIAEQIN DVKGATSDEE DEESSHEDTE
1110 1120 1130 1140 1150
NVINGPEELY GTYEYLLGMR IWSLTKERYQ KLLKQKQEKE TELENLLKLS
1160 1170 1180 1190 1200
AKDIWNTDLK AFEVGYQEFL QRDAEARGGN VPNKGSKTKG KGKRKLVDDE
1210 1220 1230 1240 1250
DYDPSKKNKK STARKGKKIK LEDKNFERIL LEQKLVTKSK APTKIKKEKT
1260 1270 1280 1290 1300
PSVSETKTEE EENAPSSTSS SSIFDIKKED KDEGELSKIS NKFKKISTIF
1310 1320 1330 1340 1350
DKMGSTSATS KENTPEQDDV ATKKNQTTAK KTAVKPKLAK KPVRKQQKVV
1360 1370 1380 1390 1400
ELSGESDLEI LDSYTDREDS NKDEDDAIPQ RSRRQRSSRA ASVPKKSYVE
1410 1420
TLELSDDSFI EDDEEENQGS DVSFNEED
Length:1,428
Mass (Da):164,215
Last modified:February 1, 1996 - v2
Checksum:i0E29EB8B89AA1387
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74N → NN in AAB36610 (PubMed:3017975).Curated1
Sequence conflicti547P → L in AAB36610 (PubMed:3017975).Curated1
Sequence conflicti837W → R in AAB36610 (PubMed:3017975).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13814 Genomic DNA Translation: AAB36610.1
AF458969 Genomic DNA Translation: AAM00518.1
AF458971 Genomic DNA Translation: AAM00530.1
AF458972 Genomic DNA Translation: AAM00536.1
X89016 Genomic DNA Translation: CAA61422.1
Z71364 Genomic DNA Translation: CAA95964.1
BK006947 Genomic DNA Translation: DAA10457.1
PIRiS57534 ISBYT2
RefSeqiNP_014311.3, NM_001182926.3

Genome annotation databases

EnsemblFungiiYNL088W; YNL088W; YNL088W
GeneIDi855636
KEGGisce:YNL088W

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13814 Genomic DNA Translation: AAB36610.1
AF458969 Genomic DNA Translation: AAM00518.1
AF458971 Genomic DNA Translation: AAM00530.1
AF458972 Genomic DNA Translation: AAM00536.1
X89016 Genomic DNA Translation: CAA61422.1
Z71364 Genomic DNA Translation: CAA95964.1
BK006947 Genomic DNA Translation: DAA10457.1
PIRiS57534 ISBYT2
RefSeqiNP_014311.3, NM_001182926.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BGWX-ray2.70A409-1201[»]
1BJTX-ray2.50A409-1201[»]
1PVGX-ray1.80A/B1-413[»]
1QZRX-ray1.90A/B1-413[»]
2RGRX-ray3.00A419-1177[»]
3L4JX-ray2.48A421-1177[»]
3L4KX-ray2.98A421-1177[»]
4GFHX-ray4.41A/F1-1177[»]
DisProtiDP00076
ProteinModelPortaliP06786
SMRiP06786
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35735, 222 interactors
DIPiDIP-2300N
IntActiP06786, 34 interactors
MINTiP06786
STRINGi4932.YNL088W

Chemistry databases

ChEMBLiCHEMBL5290

PTM databases

iPTMnetiP06786

Proteomic databases

MaxQBiP06786
PaxDbiP06786
PRIDEiP06786

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL088W; YNL088W; YNL088W
GeneIDi855636
KEGGisce:YNL088W

Organism-specific databases

EuPathDBiFungiDB:YNL088W
SGDiS000005032 TOP2

Phylogenomic databases

GeneTreeiENSGT00390000016222
HOGENOMiHOG000216693
InParanoidiP06786
KOiK03164
OMAiACKLPNY
OrthoDBiEOG092C08KH

Enzyme and pathway databases

BioCyciYEAST:G3O-33117-MONOMER
BRENDAi5.99.1.3 984
ReactomeiR-SCE-4615885 SUMOylation of DNA replication proteins

Miscellaneous databases

EvolutionaryTraceiP06786
PROiPR:P06786

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
cd00187 TOP4c, 1 hit
cd03365 TOPRIM_TopoIIA, 1 hit
Gene3Di3.30.230.10, 1 hit
3.30.565.10, 1 hit
3.40.50.670, 2 hits
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR001241 Topo_IIA
IPR013760 Topo_IIA-like_dom_sf
IPR002205 Topo_IIA_A/C
IPR013759 Topo_IIA_B_C
IPR013506 Topo_IIA_bsu_dom2
IPR018522 TopoIIA_CS
IPR031660 TOPRIM_C
IPR006171 TOPRIM_domain
IPR034157 TOPRIM_TopoII
PANTHERiPTHR10169 PTHR10169, 1 hit
PfamiView protein in Pfam
PF00204 DNA_gyraseB, 1 hit
PF00521 DNA_topoisoIV, 1 hit
PF02518 HATPase_c, 1 hit
PF01751 Toprim, 1 hit
PF16898 TOPRIM_C, 1 hit
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SM00433 TOP2c, 1 hit
SM00434 TOP4c, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
SSF56719 SSF56719, 1 hit
PROSITEiView protein in PROSITE
PS00177 TOPOISOMERASE_II, 1 hit
PS50880 TOPRIM, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTOP2_YEAST
AccessioniPrimary (citable) accession number: P06786
Secondary accession number(s): D6W191
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1996
Last modified: September 12, 2018
This is version 210 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
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